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Database: UniProt
Entry: A0A2I9EG18_9FLAO
LinkDB: A0A2I9EG18_9FLAO
Original site: A0A2I9EG18_9FLAO 
ID   A0A2I9EG18_9FLAO        Unreviewed;       364 AA.
AC   A0A2I9EG18;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   26-FEB-2020, entry version 10.
DE   RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082867};
DE            EC=2.4.1.227 {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082938};
DE   AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000256|HAMAP-Rule:MF_00033};
GN   Name=murG {ECO:0000256|HAMAP-Rule:MF_00033,
GN   ECO:0000313|EMBL:GBF20941.1};
GN   ORFNames=C21_03119 {ECO:0000313|EMBL:GBF20941.1};
OS   Arenibacter sp. C-21.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=1883406 {ECO:0000313|EMBL:GBF20941.1, ECO:0000313|Proteomes:UP000095208};
RN   [1] {ECO:0000313|EMBL:GBF20941.1, ECO:0000313|Proteomes:UP000095208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF20941.1,
RC   ECO:0000313|Proteomes:UP000095208};
RA   Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT   "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT   Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL   Genome Announc. 4:e01155-16(2016).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc
CC       subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid
CC       intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-
CC       (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|HAMAP-
CC       Rule:MF_00033, ECO:0000256|SAAS:SAAS00082940}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-
CC         trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine =
CC         beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP;
CC         Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033;
CC         EC=2.4.1.227; Evidence={ECO:0000256|HAMAP-Rule:MF_00033,
CC         ECO:0000256|SAAS:SAAS01209325};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082937}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00033}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00033,
CC       ECO:0000256|SAAS:SAAS00569248}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBF20941.1}.
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DR   EMBL; BDGL02000015; GBF20941.1; -; Genomic_DNA.
DR   RefSeq; WP_031442640.1; NZ_BDGL02000015.1.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000095208; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00033; MurG; 1.
DR   InterPro; IPR006009; GlcNAc_MurG.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   TIGRFAMs; TIGR01133; murG; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458215};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458169};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00082922};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458137};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458192};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458141};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00458209};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458156};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458181, ECO:0000313|EMBL:GBF20941.1}.
FT   DOMAIN          6..144
FT                   /note="Glyco_transf_28"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          193..327
FT                   /note="Glyco_tran_28_C"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
SQ   SEQUENCE   364 AA;  39853 MW;  7A7E08332C4BBF66 CRC64;
     MVSYRFILSG GGTGGHIYPA IAIANELKVR YPDAEFLFVG AKDRMEMEKV PQAGYKIEGL
     WISGLQRKLT FKNLMFPFKV ISSLIKAAKI VRNFKPHAVV GTGGFASGPL LKVASGKGIA
     CVLQEQNSFA GITNKLLANK VAKICVAYDG MEKFFPKDKI IKTGNPVRGD LVSMVENKEE
     ALSFFGLQPG KTTLLVLGGS LGARRVNILI EKNLPFFKEQ GIQVVWQSGK LYYEEYKKYD
     SGDVKVVAFL NRMDLAYGAA DIIISRAGAG SVSELCIVGK PVIFIPSPNV AEDHQTKNAQ
     SLVDKNAAIM VKETELDEKF GTVFSDLVNN EPLSRKLGVN IKKLAMPNAT KEIVDEIEKL
     LVQQ
//
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